Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles

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DOIResolve DOI: http://doi.org/10.1007/BF00188347
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TypeArticle
Journal titleEuropean Biophysical Journal
ISSN0175-7571
1432-1017
Volume21
Issue5
Pages345348; # of pages: 4
SubjectAlzheimer's disease; Amyloid A4; Conformational change; Octyl glucoside
AbstractThe secondary structure of a synthetic amyloid fragment des [Ala21,30]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl beta-d-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of a-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a beta-sheet conformation. Secondary structure analysis yields a predominant (> 70 %) beta-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21,30]A42 interact with the sugar-coated surface of micelles, which promotes an a to beta conformational transition.
Publication date
PublisherSpringer-Verlag
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedYes
NRC number59
NPARC number9742180
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Record identifierf398a4a2-d5ad-4952-ba7f-d6a3bc73303e
Record created2009-07-17
Record modified2016-12-19
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